5gst | pdb_00005gst
REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE
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| 5gst, resolution 2.0Å | |||||||||||||
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| Ligands: | GDN, SO4 | ||||||||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.
About this Structure
5GST is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.
Reference
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase., Ji X, Armstrong RN, Gilliland GL, Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:8241147
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